Association of SWAP-70 with the B cell antigen receptor complex

L. Masat; J. Caldwell; R. Armstrong; H. Khoshnevisan; R. Jessberger; B. Herndier; M. Wabl; D. Ferrick

doi:10.1073/pnas.040374497

Association of SWAP-70 with the B cell antigen receptor complex

L. Masat
, J. Caldwell
, R. Armstrong
, H. Khoshnevisan
, R. Jessberger
, B. Herndier
, M. Wabl
, D. Ferrick

Research output: Contribution to journal › Article › peer-review

48 Scopus citations

Abstract

SWAP-70 is a component of an enzyme complex that recombines Ig switch regions in vitro. We report here the cloning of the human cDNA and its B lymphocyte-specific expression. Although its sequence contains three nuclear localization signals, in small resting B cells, SWAP-70 is mainly found in the cytoplasm. On stimulation, SWAP-70 translocates to the nucleus. In activated, class-switching B cell cultures, it is associated with membrane IgG, but not IgM. The membrane Ig association requires a functional pleckstrin homology domain and is controlled by the C terminus. We suggest that SWAP-70 is involved not only in nuclear events but also in signaling in B cell activation.

Original language	English
Pages (from-to)	2180-2184
Number of pages	5
Journal	Proceedings of the National Academy of Sciences of the United States of America
Volume	97
Issue number	5
DOIs	https://doi.org/10.1073/pnas.040374497
State	Published - 29 Feb 2000
Externally published	Yes

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abstract = "SWAP-70 is a component of an enzyme complex that recombines Ig switch regions in vitro. We report here the cloning of the human cDNA and its B lymphocyte-specific expression. Although its sequence contains three nuclear localization signals, in small resting B cells, SWAP-70 is mainly found in the cytoplasm. On stimulation, SWAP-70 translocates to the nucleus. In activated, class-switching B cell cultures, it is associated with membrane IgG, but not IgM. The membrane Ig association requires a functional pleckstrin homology domain and is controlled by the C terminus. We suggest that SWAP-70 is involved not only in nuclear events but also in signaling in B cell activation.",

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AU - Masat, L.

AU - Caldwell, J.

AU - Armstrong, R.

AU - Khoshnevisan, H.

AU - Jessberger, R.

AU - Herndier, B.

AU - Wabl, M.

AU - Ferrick, D.

PY - 2000/2/29

Y1 - 2000/2/29

N2 - SWAP-70 is a component of an enzyme complex that recombines Ig switch regions in vitro. We report here the cloning of the human cDNA and its B lymphocyte-specific expression. Although its sequence contains three nuclear localization signals, in small resting B cells, SWAP-70 is mainly found in the cytoplasm. On stimulation, SWAP-70 translocates to the nucleus. In activated, class-switching B cell cultures, it is associated with membrane IgG, but not IgM. The membrane Ig association requires a functional pleckstrin homology domain and is controlled by the C terminus. We suggest that SWAP-70 is involved not only in nuclear events but also in signaling in B cell activation.

AB - SWAP-70 is a component of an enzyme complex that recombines Ig switch regions in vitro. We report here the cloning of the human cDNA and its B lymphocyte-specific expression. Although its sequence contains three nuclear localization signals, in small resting B cells, SWAP-70 is mainly found in the cytoplasm. On stimulation, SWAP-70 translocates to the nucleus. In activated, class-switching B cell cultures, it is associated with membrane IgG, but not IgM. The membrane Ig association requires a functional pleckstrin homology domain and is controlled by the C terminus. We suggest that SWAP-70 is involved not only in nuclear events but also in signaling in B cell activation.

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JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

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Association of SWAP-70 with the B cell antigen receptor complex

Abstract

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